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Q96FL9

- GLT14_HUMAN

UniProt

Q96FL9 - GLT14_HUMAN

Protein

Polypeptide N-acetylgalactosaminyltransferase 14

Gene

GALNT14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney.

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei151 – 1511SubstrateBy similarity
    Binding sitei176 – 1761SubstrateBy similarity
    Metal bindingi199 – 1991ManganeseBy similarity
    Binding sitei200 – 2001SubstrateBy similarity
    Metal bindingi201 – 2011ManganeseBy similarity
    Binding sitei305 – 3051SubstrateBy similarity
    Metal bindingi333 – 3331ManganeseBy similarity
    Binding sitei336 – 3361SubstrateBy similarity
    Binding sitei339 – 3391SubstrateBy similarity
    Binding sitei341 – 3411SubstrateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. O-glycan processing Source: Reactome
    3. post-translational protein modification Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_115606. O-linked glycosylation of mucins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 14 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 14
    Short name:
    GalNAc-T14
    Short name:
    pp-GaNTase 14
    Protein-UDP acetylgalactosaminyltransferase 14
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
    Gene namesi
    Name:GALNT14
    ORF Names:UNQ2434/PRO4994
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:22946. GALNT14.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134920089.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 552552Polypeptide N-acetylgalactosaminyltransferase 14PRO_0000059133Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi101 ↔ 328PROSITE-ProRule annotation
    Disulfide bondi319 ↔ 397PROSITE-ProRule annotation
    Disulfide bondi430 ↔ 449PROSITE-ProRule annotation
    Disulfide bondi476 ↔ 493PROSITE-ProRule annotation
    Disulfide bondi517 ↔ 538PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiQ96FL9.
    PaxDbiQ96FL9.
    PRIDEiQ96FL9.

    PTM databases

    PhosphoSiteiQ96FL9.

    Expressioni

    Tissue specificityi

    Detected in renal tubules (at protein level). Highly expressed in fetal and adult kidney. Widely expressed at low level. Weakly expressed in whole brain, cerebellum, thymus, lung, mammary gland, liver, stomach, small intestine, colon, pancreas, spleen, bladder, uterus, placenta, testis, ovary, skeletal muscle, leukocyte, B-cell, bone marrow, fetal brain, fetal thymus, fetal lung, fetal liver, fetal small intestine, fetal spleen, fetal skeletal and fetus. Detected in renal tubules (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ96FL9.
    BgeeiQ96FL9.
    CleanExiHS_GALNT14.
    GenevestigatoriQ96FL9.

    Organism-specific databases

    HPAiHPA010785.

    Interactioni

    Protein-protein interaction databases

    BioGridi122753. 4 interactions.
    STRINGi9606.ENSP00000288988.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96FL9.
    SMRiQ96FL9. Positions 78-547.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini27 – 552526LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini415 – 550136Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 215106Catalytic subdomain AAdd
    BLAST
    Regioni274 – 33663Catalytic subdomain BAdd
    BLAST

    Domaini

    There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
    The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.By similarity

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG239675.
    HOVERGENiHBG051699.
    KOiK00710.
    OMAiHEPEATN.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ96FL9.
    TreeFamiTF313267.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96FL9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRRLTRRLVL PVFGVLWITV LLFFWVTKRK LEVPTGPEVQ TPKPSDADWD    50
    DLWDQFDERR YLNAKKWRVG DDPYKLYAFN QRESERISSN RAIPDTRHLR 100
    CTLLVYCTDL PPTSIIITFH NEARSTLLRT IRSVLNRTPT HLIREIILVD 150
    DFSNDPDDCK QLIKLPKVKC LRNNERQGLV RSRIRGADIA QGTTLTFLDS 200
    HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFTYIE SASELRGGFD 250
    WSLHFQWEQL SPEQKARRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDM 300
    DMDIWGGENF EISFRVWMCG GSLEIVPCSR VGHVFRKKHP YVFPDGNANT 350
    YIKNTKRTAE VWMDEYKQYY YAARPFALER PFGNVESRLD LRKNLRCQSF 400
    KWYLENIYPE LSIPKESSIQ KGNIRQRQKC LESQRQNNQE TPNLKLSPCA 450
    KVKGEDAKSQ VWAFTYTQQI LQEELCLSVI TLFPGAPVVL VLCKNGDDRQ 500
    QWTKTGSHIE HIASHLCLDT DMFGDGTENG KEIVVNPCES SLMSQHWDMV 550
    SS 552

    Note: Major isoform.

    Length:552
    Mass (Da):64,321
    Last modified:December 1, 2001 - v1
    Checksum:i6F2ABAA89F482696
    GO
    Isoform 2 (identifier: Q96FL9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         100-132: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:519
    Mass (Da):60,520
    Checksum:i9028631165BC7C08
    GO
    Isoform 3 (identifier: Q96FL9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         44-99: PSDADWDDLW...NRAIPDTRHL → VWSLFFKVAG...HLQTQVFLQV

    Note: Minor isoform.

    Show »
    Length:557
    Mass (Da):64,289
    Checksum:i6968DC02A2AAF2F4
    GO
    Isoform 4 (identifier: Q96FL9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: MRRLTRRLVLPVFGVLWITVLLFFWVTKRKLEVPTGPEVQTPK → MSFPMSLARSSVPFADSGLSSSQ

    Show »
    Length:532
    Mass (Da):61,588
    Checksum:i685DB05D5597341F
    GO

    Sequence cautioni

    The sequence BAB14795.1 differs from that shown. Reason: Chimeric at the C-terminus.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti368 – 3681Q → R in BAB14795. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti469 – 4691Q → K.
    Corresponds to variant rs2288101 [ dbSNP | Ensembl ].
    VAR_033948

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4343MRRLT…VQTPK → MSFPMSLARSSVPFADSGLS SSQ in isoform 4. 1 PublicationVSP_045121Add
    BLAST
    Alternative sequencei44 – 9956PSDAD…DTRHL → VWSLFFKVAGMSPWAPQVPV SPTPPYQRGHLPTGGHLAVC HFPCLLQEAQFHLQTQVFLQ V in isoform 3. 1 PublicationVSP_011221Add
    BLAST
    Alternative sequencei100 – 13233Missing in isoform 2. 1 PublicationVSP_011222Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078144 mRNA. Translation: BAC56889.1.
    Y09324 mRNA. Translation: CAA70505.4.
    AY358758 mRNA. Translation: AAQ89118.1.
    AK022753 mRNA. Translation: BAB14227.1.
    AK024039 mRNA. Translation: BAB14795.1. Sequence problems.
    AK091313 mRNA. Translation: BAC03634.1.
    AK122747 mRNA. Translation: BAG53701.1.
    AC009301 Genomic DNA. Translation: AAX88899.1.
    AC009305 Genomic DNA. Translation: AAX93209.1.
    AC015980 Genomic DNA. Translation: AAY24301.1.
    CH471053 Genomic DNA. Translation: EAX00489.1.
    BC006269 mRNA. Translation: AAH06269.2.
    BC010659 mRNA. Translation: AAH10659.1.
    CCDSiCCDS1773.2. [Q96FL9-1]
    CCDS58705.1. [Q96FL9-4]
    CCDS58706.1. [Q96FL9-3]
    RefSeqiNP_001240755.1. NM_001253826.1. [Q96FL9-3]
    NP_001240756.1. NM_001253827.1. [Q96FL9-4]
    NP_078848.2. NM_024572.3. [Q96FL9-1]
    UniGeneiHs.468058.

    Genome annotation databases

    EnsembliENST00000324589; ENSP00000314500; ENSG00000158089. [Q96FL9-3]
    ENST00000349752; ENSP00000288988; ENSG00000158089. [Q96FL9-1]
    ENST00000406653; ENSP00000385435; ENSG00000158089. [Q96FL9-4]
    GeneIDi79623.
    KEGGihsa:79623.
    UCSCiuc002rnq.3. human.
    uc002rnr.3. human. [Q96FL9-1]
    uc002rns.3. human. [Q96FL9-3]
    uc010ezo.2. human. [Q96FL9-2]

    Polymorphism databases

    DMDMi51316071.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 14

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB078144 mRNA. Translation: BAC56889.1 .
    Y09324 mRNA. Translation: CAA70505.4 .
    AY358758 mRNA. Translation: AAQ89118.1 .
    AK022753 mRNA. Translation: BAB14227.1 .
    AK024039 mRNA. Translation: BAB14795.1 . Sequence problems.
    AK091313 mRNA. Translation: BAC03634.1 .
    AK122747 mRNA. Translation: BAG53701.1 .
    AC009301 Genomic DNA. Translation: AAX88899.1 .
    AC009305 Genomic DNA. Translation: AAX93209.1 .
    AC015980 Genomic DNA. Translation: AAY24301.1 .
    CH471053 Genomic DNA. Translation: EAX00489.1 .
    BC006269 mRNA. Translation: AAH06269.2 .
    BC010659 mRNA. Translation: AAH10659.1 .
    CCDSi CCDS1773.2. [Q96FL9-1 ]
    CCDS58705.1. [Q96FL9-4 ]
    CCDS58706.1. [Q96FL9-3 ]
    RefSeqi NP_001240755.1. NM_001253826.1. [Q96FL9-3 ]
    NP_001240756.1. NM_001253827.1. [Q96FL9-4 ]
    NP_078848.2. NM_024572.3. [Q96FL9-1 ]
    UniGenei Hs.468058.

    3D structure databases

    ProteinModelPortali Q96FL9.
    SMRi Q96FL9. Positions 78-547.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122753. 4 interactions.
    STRINGi 9606.ENSP00000288988.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    PTM databases

    PhosphoSitei Q96FL9.

    Polymorphism databases

    DMDMi 51316071.

    Proteomic databases

    MaxQBi Q96FL9.
    PaxDbi Q96FL9.
    PRIDEi Q96FL9.

    Protocols and materials databases

    DNASUi 79623.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324589 ; ENSP00000314500 ; ENSG00000158089 . [Q96FL9-3 ]
    ENST00000349752 ; ENSP00000288988 ; ENSG00000158089 . [Q96FL9-1 ]
    ENST00000406653 ; ENSP00000385435 ; ENSG00000158089 . [Q96FL9-4 ]
    GeneIDi 79623.
    KEGGi hsa:79623.
    UCSCi uc002rnq.3. human.
    uc002rnr.3. human. [Q96FL9-1 ]
    uc002rns.3. human. [Q96FL9-3 ]
    uc010ezo.2. human. [Q96FL9-2 ]

    Organism-specific databases

    CTDi 79623.
    GeneCardsi GC02M031044.
    HGNCi HGNC:22946. GALNT14.
    HPAi HPA010785.
    MIMi 608225. gene.
    neXtProti NX_Q96FL9.
    PharmGKBi PA134920089.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239675.
    HOVERGENi HBG051699.
    KOi K00710.
    OMAi HEPEATN.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q96FL9.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_115606. O-linked glycosylation of mucins.

    Miscellaneous databases

    ChiTaRSi GALNT14. human.
    GeneWikii GALNT14.
    GenomeRNAii 79623.
    NextBioi 68697.
    PROi Q96FL9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96FL9.
    Bgeei Q96FL9.
    CleanExi HS_GALNT14.
    Genevestigatori Q96FL9.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF02709. Glyco_transf_7C. 1 hit.
    PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14."
      Wang H., Tachibana K., Zhang Y., Iwasaki H., Kameyama A., Chen L., Guo J.-M., Hiruma T., Togayachi A., Kudo T., Kikuchi N., Narimatsu H.
      Biochem. Biophys. Res. Commun. 300:738-744(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Stomach.
    2. Wandall H.H., Bennett E.P.
      Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-435 (ISOFORM 2).
      Tissue: Fibroblast, Retinoblastoma and Teratocarcinoma.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Eye and Ovary.
    8. "Development of immunohistochemistry assays to assess GALNT14 and FUT3/6 in clinical trials of dulanermin and drozitumab."
      Stern H.M., Padilla M., Wagner K., Amler L., Ashkenazi A.
      Clin. Cancer Res. 16:1587-1596(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiGLT14_HUMAN
    AccessioniPrimary (citable) accession number: Q96FL9
    Secondary accession number(s): B3KV89
    , Q4ZG75, Q53SU1, Q53TJ0, Q8IVI4, Q9BRH1, Q9H827, Q9H9J8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3